CAPAM_MOUSE
ID CAPAM_MOUSE Reviewed; 706 AA.
AC P59114;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase {ECO:0000250|UniProtKB:Q9H4Z3};
DE EC=2.1.1.62 {ECO:0000250|UniProtKB:Q9H4Z3};
DE AltName: Full=Cap-specific adenosine methyltransferase {ECO:0000250|UniProtKB:Q9H4Z3};
DE Short=CAPAM {ECO:0000250|UniProtKB:Q9H4Z3};
DE AltName: Full=Phosphorylated CTD-interacting factor 1 {ECO:0000303|PubMed:30487554};
GN Name=Pcif1 {ECO:0000303|PubMed:30487554, ECO:0000312|MGI:MGI:2443858};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION.
RX PubMed=30487554; DOI=10.1038/s41422-018-0117-4;
RA Sun H., Zhang M., Li K., Bai D., Yi C.;
RT "Cap-specific, terminal N6-methylation by a mammalian m6Am
RT methyltransferase.";
RL Cell Res. 29:80-82(2019).
CC -!- FUNCTION: Cap-specific adenosine methyltransferase that catalyzes
CC formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating
CC the adenosine at the second transcribed position of capped mRNAs
CC (PubMed:30487554). Recruited to the early elongation complex of RNA
CC polymerase II (RNAPII) via interaction with POLR2A and mediates
CC formation of m6A(m) co-transcriptionally (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4Z3, ECO:0000269|PubMed:30487554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-
CC methyladenosine) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-
CC methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22744, Rhea:RHEA-
CC COMP:11518, Rhea:RHEA-COMP:11519, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85958,
CC ChEBI:CHEBI:85959; EC=2.1.1.62;
CC Evidence={ECO:0000250|UniProtKB:Q9H4Z3};
CC -!- ACTIVITY REGULATION: Cap-specific adenosine methyltransferase activity
CC is inhibited by zinc. {ECO:0000250|UniProtKB:Q9H4Z3}.
CC -!- SUBUNIT: Interacts with POLR2A; interacts with the phosphorylated C-
CC terminal domain (CTD) of POLR2A. {ECO:0000250|UniProtKB:Q9H4Z3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4Z3}.
CC -!- DOMAIN: The WW domain is sufficient for direct and specific interaction
CC with the phosphorylated CTD of RNAPII largest subunit.
CC {ECO:0000250|UniProtKB:Q9H4Z3}.
CC -!- SIMILARITY: Belongs to the CAPAM family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC031431; AAH31431.1; -; mRNA.
DR CCDS; CCDS17064.1; -.
DR RefSeq; NP_666241.1; NM_146129.3.
DR RefSeq; XP_011237796.1; XM_011239494.2.
DR RefSeq; XP_011237797.1; XM_011239495.1.
DR AlphaFoldDB; P59114; -.
DR SMR; P59114; -.
DR BioGRID; 230787; 2.
DR STRING; 10090.ENSMUSP00000039555; -.
DR iPTMnet; P59114; -.
DR PhosphoSitePlus; P59114; -.
DR EPD; P59114; -.
DR jPOST; P59114; -.
DR PaxDb; P59114; -.
DR PeptideAtlas; P59114; -.
DR PRIDE; P59114; -.
DR ProteomicsDB; 288072; -.
DR Antibodypedia; 27891; 89 antibodies from 18 providers.
DR DNASU; 228866; -.
DR Ensembl; ENSMUST00000041643; ENSMUSP00000039555; ENSMUSG00000039849.
DR GeneID; 228866; -.
DR KEGG; mmu:228866; -.
DR UCSC; uc008nwp.1; mouse.
DR CTD; 63935; -.
DR MGI; MGI:2443858; Pcif1.
DR VEuPathDB; HostDB:ENSMUSG00000039849; -.
DR eggNOG; ENOG502QVT7; Eukaryota.
DR GeneTree; ENSGT00390000016206; -.
DR HOGENOM; CLU_014369_0_0_1; -.
DR InParanoid; P59114; -.
DR OMA; VWCYPIQ; -.
DR OrthoDB; 1523233at2759; -.
DR PhylomeDB; P59114; -.
DR TreeFam; TF350163; -.
DR BioGRID-ORCS; 228866; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Pcif1; mouse.
DR PRO; PR:P59114; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P59114; protein.
DR Bgee; ENSMUSG00000039849; Expressed in embryonic brain and 206 other tissues.
DR ExpressionAtlas; P59114; baseline and differential.
DR Genevisible; P59114; MM.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016422; F:mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; ISS:UniProtKB.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; ISO:MGI.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR039881; PCIF1-like.
DR InterPro; IPR022035; PCIF1_WW.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR21727; PTHR21727; 1.
DR Pfam; PF12237; PCIF1_WW; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..706
FT /note="mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase"
FT /id="PRO_0000076088"
FT DOMAIN 43..77
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..113
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 668..686
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IKJ1"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IKJ1"
FT BINDING 552..555
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IKJ1,
FT ECO:0000250|UniProtKB:Q9H4Z3"
FT BINDING 557
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IKJ1"
FT BINDING 587..591
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IKJ1"
FT BINDING 613..615
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A0R4IKJ1,
FT ECO:0000250|UniProtKB:Q9H4Z3"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Z3"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Z3"
SQ SEQUENCE 706 AA; 80504 MW; 48646523758CF4FD CRC64;
MANENHGSPR EGASLLSHSP GTSSQSQPCS PKPVRLVQDL PEELVHAGWE KCWSRRESRP
YYFNRFTNQS LWEMPVLGQH DVLSDPLGLN ATPLPQDSSL VETPPVENKS RKRQLSEEQP
SGNGVKKPKI EIPVTPTSQS VPSSPSIPGT PTLKIWGSST EDKQAALLRP TEVYWDLDIQ
TNAVIKHRGP SEVLPPHPDV ELLRSQLILK LRQHYRELCQ QREGIEPPRE SFNRWMLERK
VVDKGCDPLL PSNCEPVVSP SMFREIMNDI PIRLSRIKFR EEAKRLLFKY AEAARRLIES
RSASPDSRKV VKWNVEDTFS WLRKEHSASK EDYMDRLEHL RRQCGPHVSA AAKDSVEGIC
SKIYHISLEY VKRIREKHLA VLKENNIPEE VEASELEPRL VYCYPVRLAV SAPPMPSVEM
HVENSVVCIR YKGEMVKVSR SYFSKLWLLY RYSCVDDSAF ERFLPRVWCL LRRYQMMFGV
GLYEGTGLQG SLPVHVFETL HRLFGVSFEC FASPLNCYFR QYCSAFPDTD GYFGSRGPCL
DFTPLSGSFE ANPPFCEELM DAMVSHFEKL LESSAEPLSF IVFIPEWREP PTPALTRMEQ
SRFKRHQLVL PAFEHEYRSG SQHICKKEEM HYKAVHNTAV LFLQNGPGFA KWGPTPERLQ
ELTAAYKQSG RSHGSSSSSS SSSSSSEAKD RDSGREQGPS REPHPT
